3hdo

X-ray diffraction
1.61Å resolution

Crystal Structure of a Histidinol-phosphate aminotransferase from Geobacter metallireducens

Released:
Entry authors: Damodharan L, Burley SK, Swaminathan S, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Reaction catalysed:
L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidinol-phosphate aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 360 amino acids
Theoretical weight: 40.72 KDa
Source organism: Geobacter metallireducens GS-15
Expression system: Escherichia coli
UniProt:
  • Canonical: Q39YP6 (Residues: 2-350; Coverage: 100%)
Gene names: Gmet_0385, hisC
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 46.37Å b: 90.075Å c: 77.522Å
α: 90° β: 92.39° γ: 90°
R-values:
R R work R free
0.199 0.185 0.202
Expression system: Escherichia coli